Search Results

Overview

Uniprot IDP50991
Protein NameT-complex protein 1 subunit delta
Gene NameCCT4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
126 SCTKLLQKGIHPTII
21 GAAGGRGKGAYQDRD
213 RDIKIVKKLGGTIDD
288 AYILNLVKQIKKTGC
292 NLVKQIKKTGCNVLL
319 LALHFLNKMKIMVIK
321 LHFLNKMKIMVIKDI
326 KMKIMVIKDIEREDI
375 NGSGKLLKITGCASP
395 IVVRGSNKLVIEEAE
42 FSNISAAKAVADAIR
489 NRHAQGEKTAGINVR
531 ETVRSILKIDDVVNT
79 NDGATILKQMQVLHP

Function

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638)

Protein Sequence

10 MPENVAPRSG 20 ATAGAAGGRG 30 KGAYQDRDKP 40 AQIRFSNISA 50 AKAVADAIRT 60 SLGPKGMDKM 70 IQDGKGDVTI 80 TNDGATILKQ 90 MQVLHPAARM 100 LVELSKAQDI 110 EAGDGTTSVV 120 IIAGSLLDSC 130 TKLLQKGIHP 140 TIISESFQKA 150 LEKGIEILTD 160 MSRPVELSDR 170 ETLLNSATTS 180 LNSKVVSQYS 190 SLLSPMSVNA 200 VMKVIDPATA 210 TSVDLRDIKI 220 VKKLGGTIDD 230 CELVEGLVLT 240 QKVSNSGITR 250 VEKAKIGLIQ 260 FCLSAPKTDM 270 DNQIVVSDYA 280 QMDRVLREER 290 AYILNLVKQI 300 KKTGCNVLLI 310 QKSILRDALS 320 DLALHFLNKM 330 KIMVIKDIER 340 EDIEFICKTI 350 GTKPVAHIDQ 360 FTADMLGSAE 370 LAEEVNLNGS 380 GKLLKITGCA 390 SPGKTVTIVV 400 RGSNKLVIEE 410 AERSIHDALC 420 VIRCLVKKRA 430 LIAGGGAPEI 440 ELALRLTEYS 450 RTLSGMESYC 460 VRAFADAMEV 470 IPSTLAENAG 480 LNPISTVTEL 490 RNRHAQGEKT 500 AGINVRKGGI 510 SNILEELVVQ 520 PLLVSVSALT 530 LATETVRSIL KIDDVVNTR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0042470 melanosome
Cellular Component GO:0044297 cell body
Cellular Component GO:0005813 centrosome
Cellular Component GO:0005832 chaperonin-containing T-complex
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005874 microtubule
Cellular Component GO:0002199 zona pellucida receptor complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0140662 ATP-dependent protein folding chaperone
Molecular Function GO:0044183 protein folding chaperone
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:1904871 positive regulation of protein localization to Cajal body
Biological Process GO:1904874 positive regulation of telomerase RNA localization to Cajal body
Biological Process GO:0032212 positive regulation of telomere maintenance via telomerase
Biological Process GO:0006457 protein folding
Biological Process GO:0050821 protein stabilization
Biological Process GO:0090666 scaRNA localization to Cajal body

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.